AUTHORS STATE THAT RESIDUE 269 IS LEU ACCORDING TO THE DENSITY MAPS.
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実験情報
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実験
実験
手法: X線回折 / 使用した結晶の数: 1
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試料調製
結晶
マシュー密度: 2.23 Å3/Da / 溶媒含有率: 44.9 %
結晶化
温度: 298 K / 手法: 蒸気拡散法, ハンギングドロップ法 詳細: protein: 9.1 mg/mL in 20 mM Tris-HCl, pH 8.0, 0.1M KCl, 10 mM pyruvate. precipitant: 24%(w/v) PEG6000, 50 mM NaH2PO4. 10 uL droplets (5uL protein + 5 uL precipitant) suspended over 1mL of ...詳細: protein: 9.1 mg/mL in 20 mM Tris-HCl, pH 8.0, 0.1M KCl, 10 mM pyruvate. precipitant: 24%(w/v) PEG6000, 50 mM NaH2PO4. 10 uL droplets (5uL protein + 5 uL precipitant) suspended over 1mL of precipitant solution, VAPOR DIFFUSION, HANGING DROP, temperature 298K
開始モデル: PDB entry 1DHP was used to get an initial MR structure solution. A better MR starting solution resulted later when PDB entry 1XXX was made available for use.
解像度: 2.2→20 Å / σ(F): 0 / 立体化学のターゲット値: Engh & Huber 詳細: The active site lysine residues (176a, 176b) form a Schiff base complex with pyruvate. Proline residues 282a, 282b are cis-prolines.
Rfactor
反射数
%反射
Selection details
Rfree
0.259
2680
9.4 %
10% of data
Rwork
0.212
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obs
0.228
26969
95.7 %
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all
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27767
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原子変位パラメータ
Biso mean: 13.105 Å2
Refine analyze
Luzzati coordinate error obs: 0.313 Å / Luzzati d res low obs: 5 Å